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Isolation, characterization, and pharmacological actions of peptide histidine valine 42, a novel prepro-vasoactive intestinal peptide-derived peptide.

Open AccessPublished:October 15, 1987DOI:https://doi.org/10.1016/S0021-9258(18)47896-9
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      The primary structure and biological activity of a novel prepro-vasoactive intestinal peptide (prepro-VIP)-derived peptide has been determined from an adrenal pheochromocytoma. The peptide was purified sufficiently for characterization by fast atom bombardment mapping after cation-exchange and reverse-phase fast protein liquid chromatography. The sequence of this novel peptide corresponds exactly to prepro-VIP-81-122 and has been designated peptide histidine valine 42 (PHV-42). Synthetic PHV-42 reduced both the force and frequency of spontaneous contractions of isolated rat uterus and was at least 12 times more potent than peptide histidine methionine (prepro-VIP-81-107), and over a hundred times more potent than noradrenaline. PHV-42 was also more potent than peptide histidine methionine in relaxing smooth muscle preparations of rat stomach and guinea pig trachea, but was approximately 4-fold less potent in reducing blood pressure than VIP. PHV-42 thus forms a separate subsystem in the VIP family of peptides and may be the most biologically active product of prepro-VIP in certain tissues such as the uterus and trachea.

      REFERENCES

        • Itoh M.
        • Obata K.
        • Yanaihara N.
        • Okamoto M.
        Nature. 1983; 304: 547-549
        • Bloom S.R.
        • Christofides N.D.
        • Delamarter J.
        • Buell G.
        • Kawashima E.
        • Polak J.M.
        Lancet. 1983; II: 1163-1165
        • Tatemoto K.
        • Mutt V.
        Proc. Natl. Acad. Sci. U. S. A. 1981; 78: 6603-6607
        • Yiangou Y.
        • Christofides N.D.
        • Blank M.A.
        • Yanaihara N.
        • Tatemoto K.
        • Bishop A.E.
        • Polak J.M.
        • Bloom S.R.
        Gastroenterology. 1985; 89: 516-524
        • Yiangou Y.
        • Requejo F.
        • Polak J.M.
        • Bloom S.R.
        Biochem. Biophys. Res. Commun. 1986; 139: 1142-1149
        • Yiangou Y.
        • Williams S.J.
        • Bishop A.E.
        • Polak J.M.
        • Bloom S.R.
        J. Clin. Endocrinol. & Metab. 1987; 64: 131-139
        • Mitchell S.J.
        • Bloom S.R.
        Gut. 1978; 19: 1043-1048
        • Morris H.R.
        • Panico M.
        • Barber M.
        • Bordoli R.S.
        • Sedgwick R.D.
        • Tyler A.
        Biochem. Biophys. Res. Commun. 1981; 101: 623-631
        • Morris H.R.
        • Panico M.
        • Karplus A.
        • Lloyd P.E.
        • Riniker B.
        Nature. 1982; 300: 643-645
        • Morris H.R.
        • Panico M.
        • Taylor G.W.
        Biochem. Biophys. Res. Commun. 1983; 117: 299-305
        • Morris H.R.
        • Panico M.
        • Etienne T.
        • Tippins J.
        • Girgis S.I.
        • MacIntyre I.
        Nature. 1984; 308: 746-748
        • Bolton T.B.
        • Lang R.J.
        • Ottesen B.
        J. Physiol. (Lond.). 1981; 318: 41-55
        • Fournier A.
        • Saunders J.K.
        • St.-Pierre S.
        Peptides (N. Y.). 1984; 5: 169-177
        • Vandermeers A.
        • Gourlet P.
        • Vandermeers-Piret M.-C.
        • Cauvin A.
        • De Neef P.
        • Rathe J.
        • Svoboda M.
        • Robberecht P.
        • Christophe J.
        Eur. J. Biochem. 1987; 164: 321-327
        • Domschke S.
        • Domschke W.
        • Bloom S.R.
        • Mitznegg P.
        • Mitchell S.J.
        • Lux G.
        • Trunz K.
        Gut. 1978; 19: 1049-1053